1mr1: Difference between revisions
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'''Crystal Structure of a Smad4-Ski Complex''' | '''Crystal Structure of a Smad4-Ski Complex''' | ||
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[[Category: Wu, J W.]] | [[Category: Wu, J W.]] | ||
[[Category: Zhang, F.]] | [[Category: Zhang, F.]] | ||
[[Category: | [[Category: Cancer]] | ||
[[Category: | [[Category: Protein interaction]] | ||
[[Category: | [[Category: Ski]] | ||
[[Category: | [[Category: Smad]] | ||
[[Category: | [[Category: Tgf-b signaling]] | ||
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Revision as of 22:37, 2 May 2008
Crystal Structure of a Smad4-Ski Complex
Overview
The Ski family of nuclear oncoproteins represses TGF-beta signaling through interactions with the Smad proteins. The crystal structure of the Smad4 binding domain of human c-Ski in complex with the MH2 domain of Smad4 reveals specific recognition of the Smad4 L3 loop region by a highly conserved interaction loop (I loop) from Ski. The Ski binding surface on Smad4 significantly overlaps with that required for binding of the R-Smads. Indeed, Ski disrupts the formation of a functional complex between the Co- and R-Smads, explaining how it could lead to repression of TGF-beta, activin, and BMP responses. Intriguingly, the structure of the Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.
About this Structure
1MR1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling., Wu JW, Krawitz AR, Chai J, Li W, Zhang F, Luo K, Shi Y, Cell. 2002 Nov 1;111(3):357-67. PMID:12419246 Page seeded by OCA on Sat May 3 01:37:04 2008
